نتایج جستجو برای: collagen type ii

تعداد نتایج: 1833950  

Journal: :Molecular medicine reports 2013
Rei Momomura Kiyohito Naito Mamoru Igarashi Taiji Watari Atsuhiko Terakado Shinji Oike Koji Sakamoto Isao Nagaoka Kazuo Kaneko

In the present study, the effect of glucosamine administration (1.5 or 3 g/day) on cartilage and bone metabolism was investigated in bicycle racers, using cartilage‑ and bone‑specific biomarkers, including C‑terminal cross‑linked telopeptides of type II collagen (CTX‑II), C‑terminal propeptides of type II procollagen (CPII), N‑terminal telopeptide...

Journal: :The Journal of Cell Biology 1977
K Von Der Mark H Von Der Mark

This work describes an approach to monitor chondrogenesis of stage-24 chick limb mesodermal cells in vitro by analyzing the onset of type II collagen synthesis with carboxymethyl-cellulose chromatography, immunofluorescence, and radioimmunoassay. This procedure allowed specific and quantitative determination of chondrocytes in the presence of fibroblasts and myoblasts, both of which synthesize ...

Journal: :The Journal of Cell Biology 1986
W Müller-Glauser B Humbel M Glatt P Sträuli K H Winterhalter P Bruckner

The tissue distribution of type II and type IX collagen in 17-d-old chicken embryo was studied by immunofluorescence using polyclonal antibodies against type II collagen and a peptic fragment of type IX collagen (HMW), respectively. Both proteins were found only in cartilage where they were co-distributed. They occurred uniformly throughout the extracellular matrix, i.e., without distinction be...

Journal: :Arthritis Research & Therapy 2009
Anne-Christine Bay-Jensen Nadine CB Tabassi Lene V Sondergaard Thomas L Andersen Frederik Dagnaes-Hansen Patrick Garnero Moustapha Kassem Jean-Marie Delaissé

INTRODUCTION The urinary level of the type II collagen degradation marker CTX-II is increased in postmenopausal women and in ovariectomised rats, suggesting that oestrogen deprivation induces cartilage breakdown. Here we investigate whether this response to oestrogen is also true for other type II collagen turnover markers known to be affected in osteoarthritis, and whether it relates to its pr...

Journal: :The Journal of biological chemistry 1992
J J Wu P E Woods D R Eyre

Type IX collagen functions in covalent cross-linkage to type II collagen in cartilage (Eyre, D. R., Apone, S., Wu, J. J., Ericsson, L. H., and Walsh, K. A. (1987) FEBS Lett. 220, 337-341). To understand this molecular relationship better, an analysis of all cross-linking sites labeled by [3H]borohydride was undertaken using the protein prepared from fetal bovine cartilage. Sequence analysis of ...

Journal: :Frontiers in bioscience : a journal and virtual library 2005
Susanne Dertinger Stephan Söeder Hubert Bösch Thomas Aigner

Skeletal dysplasias represent in vivo models of genetic defects. Achondrogenesis type II (Langer-Saldino), caused by a genetic defect in the major cartilage matrix protein, collagen type II, is a rare and severe skeletal dysplasia. It comprises a severe derangement of the fetal growth plate cartilage with subsequent ossification defects. In this study, we analyzed the matrix composition and cel...

Journal: :International journal of molecular medicine 2009
Masafumi Yoshimura Koji Sakamoto Akifumi Tsuruta Tetsuro Yamamoto Kaori Ishida Hideyo Yamaguchi Isao Nagaoka

In the present study, to investigate the effect of glucosamine, a component of glycosaminoglycans with a chondroprotective action, on articular cartilage in athletes, we looked at soccer players, who expose their joints to excessive motion and loading, and compared the levels of biomarkers for type II collagen degradation (CTX-II) and type II collagen synthesis (CPII) between soccer players and...

Journal: :The Biochemical journal 1998
W Kafienah D Brömme D J Buttle L J Croucher A P Hollander

Cathepsin K (EC 3.4.22.38) is a recently described enzyme that has been shown to cleave type I collagen in its triple helix. The aim of this study was to determine if it also cleaves type II collagen in the triple helix and to identify the helical cleavage site(s) in types I and II collagens. Soluble human and bovine type II collagen, and rat type I collagen, were incubated with cathepsin K bef...

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